Identifying Functional Cysteine Residues in the Mitochondria
| Autor: | Mattia D. Pizzagalli, Daniel W. Bak, Eranthie Weerapana |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Oxidative phosphorylation Mitochondrion medicine.disease_cause Biochemistry Mass Spectrometry Article Mitochondrial Proteins 03 medical and health sciences chemistry.chemical_compound Mitochondrial membrane transport protein 0302 clinical medicine Tandem Mass Spectrometry medicine Metallothionein Cysteine Cysteine metabolism biology General Medicine Mitochondria Cytosol Oxidative Stress 030104 developmental biology chemistry 030220 oncology & carcinogenesis Molecular Probes biology.protein Molecular Medicine Oxidation-Reduction Oxidative stress Chromatography Liquid |
| Zdroj: | ACS chemical biology. 12(4) |
| ISSN: | 1554-8937 |
| Popis: | The mitochondria are dynamic organelles that regulate oxidative metabolism and mediate cellular redox homeostasis. Proteins within the mitochondria are exposed to large fluxes in the surrounding redox environment. In particular, cysteine residues within mitochondrial proteins sense and respond to these redox changes through oxidative modifications of the cysteine thiol group. These oxidative modifications result in a loss in cysteine reactivity, which can be monitored using cysteine-reactive chemical probes and quantitative mass spectrometry (MS). Analysis of cell lysates treated with cysteine-reactive probes enable the identification of hundreds of cysteine residues, however, the mitochondrial proteome is poorly represented ( |
| Databáze: | OpenAIRE |
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